Sequence Analysis and Biochemical Characteristics of Two Non-specific Lipid Transfer Proteins from Tartary Buckwheat Seeds

Protein Pept Lett. 2023;30(6):520-529. doi: 10.2174/0929866530666230511154511.

Abstract

Introduction: Plant non-specific lipid transfer proteins (nsLTPs) play an important role in plant resistance to various stresses, and show potential applications in agriculture, industrial manufacturing, and medicine. In addition, as more and more nsLTPs are identified as allergens, nsLTPs have attracted interest due to their allergenicity. Two nsLTPs from Tartary buckwheat have been isolated and identified. There is a need to study their biochemical characteristics and allergenicity.

Objective: The study aims to investigate the biochemical characteristics of two nsLTPs from Tartary buckwheat seeds and evaluate their potential allergenicity.

Methods: Two nsLTPs derived from Tartary buckwheat, namely FtLTP1a and FtLTP1b, were produced by gene cloning, expression, and purification. Sequence analysis and biochemical characteristics of the proteins, including lipid binding ability, α-amylase inhibition activity, antifungal activity, and allergenic activity, were investigated.

Results: High-purity recombinant FtLTP1a and FtLTP1b were obtained. FtLTP1a and FtLTP1b exhibited similar lipid binding and antifungal properties. Only FtLTP1b showed weak inhibitory activity against α-amylase.

Conclusion: FtLTP1b could specifically bind IgE in the serum allergic to buckwheat and cross-react with pollen (w6). FtLTP1b is a novel allergenic member of the lipid-transfer protein 1 family found in Tartary buckwheat.

Keywords: Tartary buckwheat; antifungal activity; food allergy; gene.; lipid transfer proteins; α-amylase inhibitor.

MeSH terms

  • Allergens / chemistry
  • Antifungal Agents
  • Fagopyrum* / chemistry
  • Fagopyrum* / genetics
  • Fagopyrum* / metabolism
  • Lipids / analysis
  • Plant Proteins / chemistry
  • Seeds / chemistry
  • Sequence Analysis
  • alpha-Amylases / metabolism

Substances

  • Plant Proteins
  • Antifungal Agents
  • Allergens
  • alpha-Amylases
  • Lipids